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Items: 43

1.

DNA activates the Nse2/Mms21 SUMO E3 ligase in the Smc5/6 complex.

Varejão N, Ibars E, Lascorz J, Colomina N, Torres-Rosell J, Reverter D.

EMBO J. 2018 May 16. pii: e98306. doi: 10.15252/embj.201798306. [Epub ahead of print]

PMID:
29769404
2.

Crystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues.

Garcia-Guerrero MC, Garcia-Pardo J, Berenguer E, Fernandez-Alvarez R, Barfi GB, Lyons PJ, Aviles FX, Huber R, Lorenzo J, Reverter D.

Proc Natl Acad Sci U S A. 2018 Apr 24;115(17):E3932-E3939. doi: 10.1073/pnas.1803685115. Epub 2018 Apr 10.

PMID:
29636417
3.

Structural Mechanism for the Temperature-Dependent Activation of the Hyperthermophilic Pf2001 Esterase.

Varejão N, De-Andrade RA, Almeida RV, Anobom CD, Foguel D, Reverter D.

Structure. 2018 Feb 6;26(2):199-208.e3. doi: 10.1016/j.str.2017.12.004. Epub 2018 Jan 4.

PMID:
29307486
4.

Discovery of Mechanism-Based Inactivators for Human Pancreatic Carboxypeptidase A from a Focused Synthetic Library.

Testero SA, Granados C, Fernández D, Gallego P, Covaleda G, Reverter D, Vendrell J, Avilés FX, Pallarès I, Mobashery S.

ACS Med Chem Lett. 2017 Sep 22;8(10):1122-1127. doi: 10.1021/acsmedchemlett.7b00346. eCollection 2017 Oct 12.

PMID:
29057062
5.

Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation.

Sant'Anna R, Almeida MR, Varejāo N, Gallego P, Esperante S, Ferreira P, Pereira-Henriques A, Palhano FL, de Carvalho M, Foguel D, Reverter D, Saraiva MJ, Ventura S.

Sci Rep. 2017 Mar 24;7:44709. doi: 10.1038/srep44709.

6.

Structural analysis and evolution of specificity of the SUMO UFD E1-E2 interactions.

Liu B, Lois LM, Reverter D.

Sci Rep. 2017 Feb 6;7:41998. doi: 10.1038/srep41998.

7.

Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.

Sant'Anna R, Gallego P, Robinson LZ, Pereira-Henriques A, Ferreira N, Pinheiro F, Esperante S, Pallares I, Huertas O, Almeida MR, Reixach N, Insa R, Velazquez-Campoy A, Reverter D, Reig N, Ventura S.

Nat Commun. 2016 Feb 23;7:10787. doi: 10.1038/ncomms10787.

8.

Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization.

Haq T, Richards MW, Burgess SG, Gallego P, Yeoh S, O'Regan L, Reverter D, Roig J, Fry AM, Bayliss R.

Nat Commun. 2015 Nov 2;6:8771. doi: 10.1038/ncomms9771.

9.

ATPase-dependent control of the Mms21 SUMO ligase during DNA repair.

Bermúdez-López M, Pociño-Merino I, Sánchez H, Bueno A, Guasch C, Almedawar S, Bru-Virgili S, Garí E, Wyman C, Reverter D, Colomina N, Torres-Rosell J.

PLoS Biol. 2015 Mar 12;13(3):e1002089. doi: 10.1371/journal.pbio.1002089. eCollection 2015 Mar.

10.

Regulation of USP28 deubiquitinating activity by SUMO conjugation.

Zhen Y, Knobel PA, Stracker TH, Reverter D.

J Biol Chem. 2014 Dec 12;289(50):34838-50. doi: 10.1074/jbc.M114.601849. Epub 2014 Oct 30.

11.

RARRES3 suppresses breast cancer lung metastasis by regulating adhesion and differentiation.

Morales M, Arenas EJ, Urosevic J, Guiu M, Fernández E, Planet E, Fenwick RB, Fernández-Ruiz S, Salvatella X, Reverter D, Carracedo A, Massagué J, Gomis RR.

EMBO Mol Med. 2014 Jul;6(7):865-81. doi: 10.15252/emmm.201303675.

12.

N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case.

Graña-Montes R, Marinelli P, Reverter D, Ventura S.

Biomacromolecules. 2014 Apr 14;15(4):1194-203. doi: 10.1021/bm401776z. Epub 2014 Mar 6.

PMID:
24564702
13.

Structural insights into the SENP6 Loop1 structure in complex with SUMO2.

Alegre KO, Reverter D.

Protein Sci. 2014 Apr;23(4):433-41. doi: 10.1002/pro.2425. Epub 2014 Mar 10.

14.

Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia coli strains displaying an SLR fold.

Urosev D, Ferrer-Navarro M, Pastorello I, Cartocci E, Costenaro L, Zhulenkovs D, Maréchal JD, Leonchiks A, Reverter D, Serino L, Soriani M, Daura X.

BMC Struct Biol. 2013 Oct 7;13:19. doi: 10.1186/1472-6807-13-19.

15.

SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation.

O'Rourke JG, Gareau JR, Ochaba J, Song W, Raskó T, Reverter D, Lee J, Monteys AM, Pallos J, Mee L, Vashishtha M, Apostol BL, Nicholson TP, Illes K, Zhu YZ, Dasso M, Bates GP, Difiglia M, Davidson B, Wanker EE, Marsh JL, Lima CD, Steffan JS, Thompson LM.

Cell Rep. 2013 Jul 25;4(2):362-75. doi: 10.1016/j.celrep.2013.06.034. Epub 2013 Jul 18.

16.

A noncanonical mechanism of carboxypeptidase inhibition revealed by the crystal structure of the Tri-Kunitz SmCI in complex with human CPA4.

Alonso del Rivero M, Reytor ML, Trejo SA, Chávez MA, Avilés FX, Reverter D.

Structure. 2013 Jul 2;21(7):1118-26. doi: 10.1016/j.str.2013.04.021. Epub 2013 Jun 6.

17.

Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.

Gallego P, Velazquez-Campoy A, Regué L, Roig J, Reverter D.

J Biol Chem. 2013 Apr 26;288(17):12283-94. doi: 10.1074/jbc.M113.459149. Epub 2013 Mar 12.

18.

Structural characterization of the enzymes composing the arginine deiminase pathway in Mycoplasma penetrans.

Gallego P, Planell R, Benach J, Querol E, Perez-Pons JA, Reverter D.

PLoS One. 2012;7(10):e47886. doi: 10.1371/journal.pone.0047886. Epub 2012 Oct 17.

19.

The novel structure of a cytosolic M14 metallocarboxypeptidase (CCP) from Pseudomonas aeruginosa: a model for mammalian CCPs.

Otero A, Rodríguez de la Vega M, Tanco S, Lorenzo J, Avilés FX, Reverter D.

FASEB J. 2012 Sep;26(9):3754-64. doi: 10.1096/fj.12-209601. Epub 2012 May 29.

PMID:
22645247
20.

Native structure protects SUMO proteins from aggregation into amyloid fibrils.

Sabate R, Espargaro A, Graña-Montes R, Reverter D, Ventura S.

Biomacromolecules. 2012 Jun 11;13(6):1916-26. doi: 10.1021/bm3004385. Epub 2012 May 25.

PMID:
22559198
21.

Crystal structure of novel metallocarboxypeptidase inhibitor from marine mollusk Nerita versicolor in complex with human carboxypeptidase A4.

Covaleda G, del Rivero MA, Chávez MA, Avilés FX, Reverter D.

J Biol Chem. 2012 Mar 16;287(12):9250-8. doi: 10.1074/jbc.M111.330100. Epub 2012 Jan 31.

22.

Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2.

Gareau JR, Reverter D, Lima CD.

J Biol Chem. 2012 Feb 10;287(7):4740-51. doi: 10.1074/jbc.M111.321141. Epub 2011 Dec 22.

23.

Swapping small ubiquitin-like modifier (SUMO) isoform specificity of SUMO proteases SENP6 and SENP7.

Alegre KO, Reverter D.

J Biol Chem. 2011 Oct 14;286(41):36142-51. doi: 10.1074/jbc.M111.268847. Epub 2011 Aug 30.

24.

DYNLL/LC8 protein controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9.

Regué L, Sdelci S, Bertran MT, Caelles C, Reverter D, Roig J.

J Biol Chem. 2011 May 20;286(20):18118-29. doi: 10.1074/jbc.M110.209080. Epub 2011 Mar 22.

25.

Preparation of SUMO proteases and kinetic analysis using endogenous substrates.

Reverter D, Lima CD.

Methods Mol Biol. 2009;497:225-39. doi: 10.1007/978-1-59745-566-4_15. Review.

26.

Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7.

Lima CD, Reverter D.

J Biol Chem. 2008 Nov 14;283(46):32045-55. doi: 10.1074/jbc.M805655200. Epub 2008 Sep 16.

27.

Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates.

Reverter D, Lima CD.

Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. Epub 2006 Nov 12.

PMID:
17099700
28.
29.

Structure of a complex between Nedd8 and the Ulp/Senp protease family member Den1.

Reverter D, Wu K, Erdene TG, Pan ZQ, Wilkinson KD, Lima CD.

J Mol Biol. 2005 Jan 7;345(1):141-51.

PMID:
15567417
30.
31.

Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.

Reverter D, Maskos K, Tan F, Skidgel RA, Bode W.

J Mol Biol. 2004 Apr 23;338(2):257-69.

PMID:
15066430
32.

Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins.

Hemelaar J, Borodovsky A, Kessler BM, Reverter D, Cook J, Kolli N, Gan-Erdene T, Wilkinson KD, Gill G, Lima CD, Ploegh HL, Ovaa H.

Mol Cell Biol. 2004 Jan;24(1):84-95.

33.

Flexibility analysis and structure comparison of two crystal forms of calcium-free human m-calpain.

Reverter D, Braun M, Fernandez-Catalan C, Strobl S, Sorimachi H, Bode W.

Biol Chem. 2002 Sep;383(9):1415-22.

PMID:
12437134
34.

Crystal structure of a novel mid-gut procarboxypeptidase from the cotton pest Helicoverpa armigera.

Estébanez-Perpiñá E, Bayés A, Vendrell J, Jongsma MA, Bown DP, Gatehouse JA, Huber R, Bode W, Avilés FX, Reverter D.

J Mol Biol. 2001 Oct 26;313(3):629-38.

PMID:
11676544
35.

The structure of calcium-free human m-calpain: implications for calcium activation and function.

Reverter D, Sorimachi H, Bode W.

Trends Cardiovasc Med. 2001 Aug;11(6):222-9. Review.

PMID:
11673052
36.

Structural basis for possible calcium-induced activation mechanisms of calpains.

Reverter D, Strobl S, Fernandez-Catalan C, Sorimachi H, Suzuki K, Bode W.

Biol Chem. 2001 May;382(5):753-66.

PMID:
11517928
37.

Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2.

Reverter D, Fernández-Catalán C, Baumgartner R, Pfänder R, Huber R, Bode W, Vendrell J, Holak TA, Avilés FX.

Nat Struct Biol. 2000 Apr;7(4):322-8.

PMID:
10742178
38.

A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis. Isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization.

Reverter D, Vendrell J, Canals F, Horstmann J, Avilés FX, Fritz H, Sommerhoff CP.

J Biol Chem. 1998 Dec 4;273(49):32927-33.

39.

Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B.

Aloy P, Catasús L, Villegas V, Reverter D, Vendrell J, Avilés FX.

Biol Chem. 1998 Feb;379(2):149-55.

PMID:
9524066
40.

Overexpression of human procarboxypeptidase A2 in Pichia pastoris and detailed characterization of its activation pathway.

Reverter D, Ventura S, Villegas V, Vendrell J, Avilés FX.

J Biol Chem. 1998 Feb 6;273(6):3535-41.

41.

Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2.

Reverter D, García-Sáez I, Catasús L, Vendrell J, Coll M, Avilés FX.

FEBS Lett. 1997 Dec 22;420(1):7-10.

42.
43.

Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2.

Villegas V, Azuaga A, Catasús L, Reverter D, Mateo PL, Avilés FX, Serrano L.

Biochemistry. 1995 Nov 21;34(46):15105-10.

PMID:
7578124

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